Dynamic transport of SNARE proteins in the Golgi apparatus Journal Article


Authors: Cosson, P.; Ravazzola, M.; Varlamov, O.; Sollner, T. H.; Diliberto, M.; Volchuk, A.; Rothman, J. E.; Orci, L.
Article Title: Dynamic transport of SNARE proteins in the Golgi apparatus
Abstract: Localization of a membrane protein in a subcellular compartment can be achieved by its retention in the compartment or by its continuous transport toward this compartment. Previous results have suggested that specific enzymes are localized in the Golgi apparatus at least in part by selective retention and exclusion from transport vesicles. However, the function of some Golgi SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins is not compatible with their exclusion from transport vesicles. To help understand the mechanism accounting for the localization of SNARE proteins in the Golgi apparatus, we analyzed their lateral distribution in the Golgi cisternae and their incorporation into transport vesicles. According to our results, all SNARE proteins are efficiently incorporated into transport vesicles, indicating that the localization of SNARE proteins in the Golgi apparatus is not based on a static retention mechanism. Detailed analysis suggested that incorporation into transport vesicles was more efficient for SNARE proteins restricted to the cis face of the Golgi as compared with SNAREs present at the trans face. Furthermore, overexpression of a cis-Golgi SNARE protein altered concomitantly its incorporation in transport vesicles and its intra-Golgi localization. These observations suggest that, contrary to resident Golgi enzymes, SNARE proteins are localized in the Golgi apparatus as the result of a dynamic transport equilibrium. © 2005 by The National Academy of Sciences of the USA.
Keywords: controlled study; human cell; nonhuman; protein function; protein localization; animal cell; animals; microscopy, electron; gene overexpression; blotting, western; fluorescent antibody technique; protein transport; protein secretion; biological transport; cis trans isomerism; secretion; golgi complex; cho cells; cricetinae; cricetulus; glycosyltransferase; vesicular transport; snare protein; transport vesicle; golgi apparatus; transport vesicles; snare proteins; cisternal maturation; membrane sorting
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 102
Issue: 41
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 2005-10-11
Start Page: 14647
End Page: 14652
Language: English
DOI: 10.1073/pnas.0507394102
PUBMED: 16199514
PROVIDER: scopus
PMCID: PMC1253604
DOI/URL:
Notes: --- - "Cited By (since 1996): 16" - "Export Date: 24 October 2012" - "CODEN: PNASA" - "Source: Scopus"
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  1. Thomas H Sollner
    65 Sollner
  2. Allen Volchuk
    10 Volchuk
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